- 1) Brurberg, M.B., Eijsink, V.G., Haandrikman, A.J., Venema, G., and Nes, I.F., Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing. Microbiology, 141, 123-131 (1995).
- 2) Brurberg, M.B., Eijsink, V.G., and Nes, I.F., Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product. FEMS Microbiol. Lett., 124, 399-404 (1994).
- 3) Fuchs, R.L., McPherson, S.A., and Drahos, D.J., Cloning of a Serratia marcescens gene encoding chitinase. Appl. Environ. Microbiol., 51, 504-509 (1986).
- 4) Gal, S.W., Choi, J.Y., Kim, C.Y., Cheong, Y.H., Choi, Y.J., Bahk, J.D., Lee, S.Y., and Cho, M.J., Isolation and characterization of the 54-kDa and 22-kDa chitinase genes of Serratia marcescens KCTC2172. FEMS Microbiol. Lett., 151, 197-204 (1997).
- 5) Harpster, M.H. and Dunsmuir, P., Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466. Nucleic Acids Res., 17, 5395 (1989).
- 6) Jones, J.D.G., Grady, K.L., Suslow, T.V., and Bedbrook, J.R., Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J., 5, 467-473 (1986).
- 7) Watanabe, T., Kimura, K., Sumiya, T., Nikaidou, N., Suzuki, K., Suzuki, M., Taiyoji, M., Ferrer, S., and Regue, M., Genetic analysis of the chitinase system of Serratia marcescens 2170. J. Bacteriol., 179, 7111-7117 (1997).
- 8) Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A.B., Chet, I., Wilson, K.S., and Vorgias, C.E., Crystal structure of a bacterial chitinase at 2.3 Å resolution. Structure, 2, 1169-1180 (1994).
- 9) Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B., and Watanabe, T., The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem. J., 343, 587-596 (1999).
- 10) Gal, S.W., Choi, J.Y., Kim, C.Y., Cheong, Y.H., Choi, Y.J., Lee, S.Y., Bahk, J.D., and Cho, M.J., Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme. FEMS Microbiol. Lett., 160, 151-158 (1998).
- 11) Suzuki, K., Suzuki, M., Taiyoji, M., Nikaidou, N., and Watanabe, T., Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170. Biosci. Biotechnol. Biochem., 62, 128-135 (1998).
- 12) Kolbe, S., Fischer, S., Becirevic, A., Hinz, P., and Schrempf, H., The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene. Microbiology, 144, 1291-1297 (1998).
- 13) Schnellmann, J., Zeltines, A., Blaak, H., and Schrempf, H., The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms. Mol. Microbiol., 13, 807-819 (1994).
- 14) Alam, M.M., Mizutani, T., Isono, M., Nikaidou, N., and Watanabe, T., Three chitinase genes (chiA, chiC and chiD) comprise the chitinase system of Bacillus circulans WL-12. J. Ferment. Bioeng., 82, 28-36 (1996).
- 15) Miyashita, K., Fujii, T., Watanabe, A., and Ueno, H., Nucleotide sequence and expression of a gene (chiB) for a chitinase from Streptomyces lividans. J. Ferment. Bioeng., 83, 26-31 (1997).
- 16) Shiro, M., Ueda, M., Kawaguchi, T., and Arai, M., Cloning of a cluster of chitinase genes from Aeromonas sp. No. 10S-24. Biochimi. Biophysi. Acta, 1305, 44-48 (1996).
- 17) Tsujibo, H., Orikoshi, H., Shiotani, K., Hayashi, M., Umeda, J., Miyamoto, K., Imada, C., Okami, Y., and Inamori, Y., Characterization of chitinase C from a marine bacterium, Alteromonas sp. strain O-7, and its corresponding gene and domain structure Appl. Environ. Microbiol., 64, 472-478 (1998).
- 18) Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
- 19) Watanabe, T., Kanai, R., Kawase, T., Tanabe, T., Mitsutomi, M., Sakuda, S., and Miyashita, K., Family 19 chitinases of Streptomyces species: characterization and distribution. Microbiology, 145, 3353-3363 (1999).
- 20) Rubirés, X., Saigi, F., Piqué, N., Clinent, N., Merino, S., Albertí, S., Tomás, J.M., and Regué, M., A gene (wbbL) from Serratia marcescens N28b (O4) complements the rfb-50 mutation of Escherichia coli K-12. J. Bacteriol., 179, 7581-7586 (1997).
- 21) Imoto, T. and Yagishita, K., A simple activity measurement of lysozyme. Agr. Biol. Chem., 35, 1154-1156 (1971).
- 22) Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
- 23) Ames, G.F., Resolution of bacterial proteins by polyacrylamide gel electro-phoresis on slabs. Membrane, soluble, and periplasmic fractions. J. Biol. Chem., 249, 634-644 (1974).
- 24) Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
- 25) Watanabe, T., Oyanagi, W., Suzuki, K., and Tanaka, H., Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol., 172, 4017-4022 (1990).
- 26) Silhavy, T.J., Berman, M.L., and Enquist, L.W., Experiments with gene fusions. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. (1984).
- 27) Miller, V.L. and Mekalanos, J.J., A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol., 170, 2575-2583 (1988).
- 28) Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038 (1987).
- 29) Jeuniaux, C., Chitinase. Methods Enzymol., 8, 644-650 (1966).
- 30) Schell, M.A., Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol., 47, 597-626 (1993).
- 31) Tao, K., Fujita, N., and Ishihama, A., Involvement of the RNA polymerase α subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein. Mol. Microbiol., 7, 859-864 (1993).
- 32) Thomas, M.S. and Glass, R.E., Escherichia coli rpoA mutation which impairs transcription of positively regulated system. Mol. Microbiol., 5, 2719-2725 (1991).
- 33) Goethals, K., Montagu, M.V., and Holsters, M., Conserved motif in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins. Proc. Natl. Acad. Sci. USA, 89, 1646-1650 (1992).
- 34) Hryniewicz, M.M. and Kredich, N.M., Hydroxyl radical footprints and half-site arrangements of binding site for the CysB transcriptional activator of Salmonella typhimurium. J. Bacteriol., 177, 2343-2353 (1995).
- 35) Toledano, M.B., Kullik, I., Trinh, F., Baird, P.T., Schneider, T.D., and Storz, G., Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell, 78, 897-909 (1994).
- 36) Ni, X. and Westpheling, J., Direct repeat sequences in the Streptomyces chitinase-63 promoter direct both glucose repression and chitin induction. Proc. Natl. Acad. Sci. USA, 94, 13116-13121 (1997).
- 37) Saito, A., Fujii, T., Yoneyama, T., Redenbach, M., Ohno, T., Watanabe, T., and Miyashita, K., High-multiplicity of chitinase gene in Streptomyces coelicolor A3 (2). Biosci. Biotechnol. Biochem., 63, 710-718 (1999).
- 38) Tsujibo, H., Endo, H., Minoura, K., Miyamoto, K., and Inamori, Y., Cloning and sequence analysis of the gene encoding a thermostable chitinase from Streptomyces thermoviolaceus OPC-520. Gene, 134, 113-117 (1993).
- 39) Tsujibo, H., Kondo, N., Tanaka, K., Miyamoto, K., Baba, N., and Inamori, Y., Molecular analysis of the gene encoding a novel transglycosylative enzyme from Altermonas sp. strain O-7 and its physiological role in the chitinolytic system. J. Bacteriol., 181, 5461-5466 (1999).
Full access
LysR-type Transcriptional Regulator ChiR Is Essential for Production of All Chitinases and a Chitin-Binding Protein, CBP21, in Serratia marcescens 2170
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.